Product Details

Purity

Greater than 85% as determined by SDS-PAGE.

Target Names

RECQL

Uniprot No.

P46063

Research Area

Epigenetics and Nuclear Signaling

Alternative Names

RECQL; RECQ1; RECQL1; ATP-dependent DNA helicase Q1; EC 3.6.4.12; DNA helicase; RecQ-like type 1; RecQ1; DNA-dependent ATPase Q1; RecQ protein-like 1

Species

Homo sapiens (Human)

Source

E.coli

Expression Region

1-649aa

Target Protein Sequence

MASVSALTEELDSITSELHAVEIQIQELTERQQELIQKKKVLTKKIKQCLEDSDAGASNEYDSSPAAWNKEDFPWSGKVKDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISATMLNASSSKEHVKWVHAEMVNKNSELKLIYVTPEKIAKSKMFMSRLEKAYEARRFTRIAVDEVHCCSQWGHDFRPDYKALGILKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFNRPNLYYEVRQKPSNTEDFIEDIVKLINGRYKGQSGIIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGRDDMKADCILYYGFGDIFRISSMVVMENVGQQKLYEMVSYCQNISKCRRVLMAQHFDEVWNSEACNKMCDNCCKDSAFERKNITEYCRDLIKILKQAEELNEKLTPLKLIDSWMGKGAAKLRVAGVVAPTLPREDLEKIIAHFLIQQYLKEDYSFTAYATISYLKIGPKANLLNNEAHAITMQVTKSTQNSFRAESSQTCHSEQGDKKMEEKNSGNFQKKAANMLQQSGSKNTGAKKRKIDDA
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Mol. Weight

73.5 kDa

Protein Length

Full Length

Tag Info

Tag-Free

Form

Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

3-7 business days

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet & COA

Please contact us to get it.

Description

The production of this Recombinant Human VP35 protein began at the genetic level, where the coding sequence for the VP35 protein was first isolated and cloned into an expression plasmid vector. Recombinant DNA technology was used in the process. Next step was cloning. The expression vector must be introduced into the host cell (E.coli) so that the cells could be cultured and expressed the desired RECQL protein. And we finally got the recombinant RECQL protein with the purity of 85%+ determined by SDS-PAGE.

Active adenosine triphosphate (ATP) is required for inflammasome activation. Intracellular ATP is released after cellular stress and/or activation, and purinergic signaling has been shown to modulate inflammation and immunity. In the extracellular space, ATP is rapidly hydrolysed in a stepwise manner to ADP, AMP (adenosine monophosphate) and adenosine by ectoenzymes. Extracellular ATP (eATP) signals through both ATP-gated ion channels P2X and G protein-coupled receptor (GPCR) P2Y membrane receptors, whereas ADP signals through P2Y receptors and adenosine through P1 receptors (or A receptors). Extracellular adenosine level is the result of adenosine production from extracellular ATP and ADP, its degradation into inosine and its reuptake by cells. Both ATP and adenosine can be transported outside of the cell via diffusion or active transport, whereas only adenosine can enter the cells through adenosine transporters. Intracellular adenosine is converted to ATP via phosphorylation steps mediated by adenosine kinase (AK) and AMP kinase (AMPK). ATP-derived adenosine and its subsequent signalling through P1 receptors have beneficial roles in acute disease states.

Target Background

Function

DNA helicase that may play a role in the repair of DNA that is damaged by ultraviolet light or other mutagens. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction.

Gene References into Functions

Based on the current genetic data, both RECQL p.I156M and POLG p.L392V represent novel breast cancer predisposing alleles. PMID: 29341116
the RECQL:c.1667_1667 + 3delAGTA mutation in Polish women was not correlated to breast cancer susceptibility PMID: 29351780
Study detected five different RECQL mutation in six unrelated breast cancer patients. The identified mutations include one frame-shift deletion, two splicing site mutation and one nonsense mutation. PMID: 27125668
RECQ1 is significantly overexpressed in multiple myeloma cells vs normal plasma cells. Increased RECQ1 expression is associated with poor prognosis. Its knockdown inhibits cell growth, increases apoptosis, and promotes DNA ds-breaks. Its overexpression protects against melphalan and bortezomib. It interacts with PARP1 and its loss sensitizes to PARP inhibitors. PMID: 28186131
Data indicate that RECQL* c.1667_1667+3delAGTA is not a high-risk mutation for breast cancer though it could represent a moderate-risk breast cancer susceptibility allele.[meta-analysis] PMID: 27832498
The authors have discovered a major sub-pathway of conventional long-patch base excision repair that involves formation of a 9-nucleotide gap 5' to the lesion. This new sub-pathway is mediated by RECQ1 DNA helicase and ERCC1-XPF endonuclease in cooperation with PARP1 poly(ADP-ribose) polymerase and RPA. PMID: 28373211
We conclude that RECQL1 has prognostic and predictive significance in breast cancers. PMID: 27837030
Our results indicate that the zinc binding motif in the RQC domain of RECQ1 is a key structural element that is essential for the structure-functions of RECQ1. PMID: 27248010
Knockdown of RECQ1 significantly suppressed lung cancer cell proliferation, migration and invasion. PMID: 27565844
To better understand the roles of RECQ1, two AL mutants (W227A and F231A) in full-length RECQ1 were characterized biochemically and genetically PMID: 26455304
RECQL is a new breast cancer susceptibility gene. PMID: 26125302
RECQL is a DNA helicase in breast cancer [editorial] PMID: 26387136
RECQ1 A159C genotype may be a prognostic or predictive factor for resectable pancreatic cancer patients who are treated with adjuvant 5-FU before and after 5-FU-based chemoradiation. PMID: 26725729
RECQL is a potential breast cancer susceptibility gene; mutations in this gene contribute to familial breast cancer development. PMID: 25945795
RECQL1 is a prognostic factor for epithelial ovarian cancer and contributes to potential malignancy by inhibiting apoptosis. PMID: 25424877
A novel function of RECQ1 is identified: in gene regulation and indicates that RECQ1 contributes to tumor development and progression, in part, by regulating the expression of key genes that promote cancer cell migration, invasion and metastasis. PMID: 25483193
RECQL is a breast cancer susceptibility gene. PMID: 25915596
we show that RECQ1 can form what appears to be a flat, homotetrameric complex and propose that RECQ1 tetramers are involved in Holliday junction recognition PMID: 25831490
our results provide first indication of nonredundant participation of WRN and RECQ1 in protection from the potentially carcinogenic effects PMID: 25228686
results indicate that RECQL1 plays an important regulatory role in cancer cell proliferation and tumor progression PMID: 24854846
The stimulation of helicase-catalyzed protein displacement is observed with the DNA helicase RECQ1, suggesting a conserved functional interaction of RPA-interacting helicases. PMID: 24895130
RECQL1 may participate in the same pathway as WRN, probably in telomere replication. PMID: 24623817
a crucial role for RECQ1 at naturally occurring fork stalling sites and implicate RECQ1 in mechanisms underlying common fragile site instability in cancer. PMID: 23601052
RECQL1 expression was exceptionally high in rapidly growing ovarian cancer cells. PMID: 23951333
An interaction of RECQ1 with Ku70/80 and a role of the human RecQ helicase in double-strand break repair through nonhomologous end-joining. PMID: 23650516
RECQ1 might have a similar role to that of WRN in helping cells deal with stalled replication forks. PMID: 23095637
RECQ1 promotes restart of DNA replication forks reversed by DNA topoisomerase I inhibition. PMID: 23396353
The data suggested that HomolD-containing promoters require the RNA polymerase II machinery and the proteins DDB1 and RECQL for accurate transcription. PMID: 22705827
Data show that RECQ1 associates with PARP-1 in nuclear extracts and exhibits direct protein interaction in vitro. PMID: 22542292
RAD54 that lacks helicase activity is more efficient in DNA heterology bypass than BLM or REQ1 helicases. PMID: 22356911
RECQ1 might represent a new suitable target for anti cancer therapies aimed to arrest cell proliferation in brain gliomas. PMID: 21752281
The beta-hairpin is a key structural element that controls not only the enzymatic activity of RECQ1, but also the balance between the multiple oligomeric states of the protein. PMID: 21059676
Histological data reveal the potential of RecQL1 as a biological marker predicting the malignancy and progression of liver cancer. PMID: 20198302
These results indicate that RECQ1 and RECQ4 are integral components of the human replication complex and play distinct roles in DNA replication initiation and replication fork progression in vivo. PMID: 20065033
Molecular cloning of a splicing variant of human RECQL helicase. PMID: 12419324
characterization of DNA-unwinding activity PMID: 12419808
RECQ1 alone is able to unwind short DNA duplexes (<110 bp), whereas considerably longer substrates (501 bp) can be unwound only in the presence of human replication protein A (hRPA) PMID: 15096578
RECQ1 has a role in a pathway involving mismatch repair factors PMID: 15886194
analysis of enzymatic properties of the RECQ1 helicase and DNA unwinding and strand annealing activities PMID: 15899892
Identification of RecQL1 as a predominant ATP-dependent, Holliday junction branch migrator present in human nuclear extracts. PMID: 16260474
Our findings suggest that higher-order oligomers are associated with DNA strand annealing, and lower-order oligomers with DNA unwinding. PMID: 17227144
RecQ DNA helicase resolves genetic recombination and suppressive aberrant recombination. PMID: 17483412
Results support that endogenous DNA damage that occurs during DNA replication and remains unrepaired in cancer cells due to RecQL1 silencing induces cancer cell-specific mitotic catastrophe through a less-strict checkpoint in cancer than in normal cells. PMID: 17953710
results provide the first evidence for a role of human RECQ1 in the response to DNA damage and chromosomal stability maintenance and point to the vital importance of RECQ1 in genome homeostasis PMID: 18074021
Human RecQ helicases, BLM and RECQ1, display distinct DNA substrate specificities PMID: 18448429
properties of the RECQ1 helicase may have important implications for the function of RECQ1 in maintenance of genomic stability PMID: 18495662
A crystal structure of a truncated form of the human RECQ1 protein with Mg-ADP, is presented. PMID: 19151156
Topoisomerase I and RecQL1 promote the lytic reactivation of Epstein-Barr virus. PMID: 19494003

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Subcellular Location

Nucleus.

Protein Families

Helicase family, RecQ subfamily

Tissue Specificity

High expression in heart, lung, skeletal muscle and kidney, low expression in brain.

Database Links

HGNC: 9948

OMIM: 600537

KEGG: hsa:5965

STRING: 9606.ENSP00000395449

UniGene: Hs.235069

Code	CSB-EP019537HU
Abbreviation	Recombinant Human RECQL protein
MSDS	MSDS Datasheet
Size	$554
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Image	(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Recombinant Human ATP-dependent DNA helicase Q1 (RECQL)

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